Zinc in PDB 1h3n: Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate

All present enzymatic activity of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate:
6.1.1.4;

The structure of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate, PDB code: 1h3n was solved by S.Cusack, A.Yaremchuk, M.Tukalo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.63 / 2.0
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	102.410, 155.590, 176.300, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 23.1

The binding sites of Zinc atom in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate (pdb code 1h3n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate, PDB code: 1h3n:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1817 b:42.4 occ:1.00 SG A:CYS439 2.3 39.2 1.0 SG A:CYS487 2.3 46.2 1.0 SG A:CYS484 2.3 40.4 1.0 SG A:CYS442 2.3 41.6 1.0 CB A:CYS484 3.1 36.7 1.0 CB A:CYS439 3.2 38.6 1.0 CB A:CYS442 3.2 38.3 1.0 CB A:CYS487 3.3 45.6 1.0 N A:CYS487 3.7 46.4 1.0 N A:CYS442 3.9 36.4 1.0 CA A:CYS487 4.1 46.9 1.0 CA A:CYS442 4.2 36.5 1.0 O A:HOH2335 4.3 44.5 1.0 CB A:LYS486 4.5 46.2 1.0 CA A:CYS484 4.6 38.0 1.0 CA A:CYS439 4.7 37.2 1.0 N A:GLY488 4.7 47.6 1.0 C A:LYS486 4.8 45.9 1.0 CB A:ALA441 4.8 36.3 1.0 C A:CYS487 4.9 47.6 1.0 CG2 A:VAL445 4.9 34.4 1.0 C A:ALA441 4.9 37.2 1.0

Zinc binding site 2 out of 2 in the Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Leucyl-Trna Synthetase From Thermus Thermophilus Complexed with A Sulphamoyl Analogue of Leucyl-Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1818 b:35.4 occ:1.00 ND1 A:HIS179 2.2 38.0 1.0 SG A:CYS162 2.3 37.4 1.0 SG A:CYS176 2.4 34.7 1.0 SG A:CYS159 2.4 36.4 1.0 CE1 A:HIS179 3.1 38.6 1.0 CG A:HIS179 3.3 41.9 1.0 CB A:CYS176 3.3 38.1 1.0 CB A:CYS162 3.4 38.6 1.0 CB A:CYS159 3.5 37.7 1.0 CB A:HIS179 3.7 41.4 1.0 N A:CYS162 3.7 39.0 1.0 CA A:CYS162 4.1 37.7 1.0 N A:HIS179 4.2 44.4 1.0 CB A:LYS161 4.3 44.9 1.0 NE2 A:HIS179 4.3 40.9 1.0 CD2 A:HIS179 4.4 40.8 1.0 CB A:ARG178 4.4 41.5 1.0 CA A:HIS179 4.6 45.0 1.0 C A:LYS161 4.6 41.0 1.0 CA A:CYS176 4.8 38.0 1.0 CA A:CYS159 4.9 38.2 1.0 CD1 A:LEU166 4.9 31.1 1.0 CA A:LYS161 4.9 41.9 1.0 C A:ARG178 4.9 43.6 1.0

S.Cusack, A.Yaremchuk, M.Tukalo. The 2A Structure of Leucyl-Trna Synthetase and Its Complex with A Leucyl-Adenylate Analogue Embo J. V. 19 2351 2000.
ISSN: ISSN 0261-4189
PubMed: 10811626
DOI: 10.1093/EMBOJ/19.10.2351